Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation.

Prions are transmissible, propagating alternative states of proteins. Prions in budding yeast propagate heritable phenotypes and can function in large-scale gene regulation, or in some cases occur as diseases of yeast. Other 'prionogenic' proteins are likely prions that have been determine...

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Autores principales:	Djamel Harbi, Paul M Harrison
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/cfab7fbcd2d64446870f7978378a3f51
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spelling	oai:doaj.org-article:cfab7fbcd2d64446870f7978378a3f512021-11-11T08:21:03ZInteraction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation.1932-620310.1371/journal.pone.0100615https://doaj.org/article/cfab7fbcd2d64446870f7978378a3f512014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24972093/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Prions are transmissible, propagating alternative states of proteins. Prions in budding yeast propagate heritable phenotypes and can function in large-scale gene regulation, or in some cases occur as diseases of yeast. Other 'prionogenic' proteins are likely prions that have been determined experimentally to form amyloid in vivo, and to have prion-like domains that are able to propagate heritable states. Furthermore, there are over 300 additional 'prion-like' yeast proteins that have similar amino-acid composition to prions (primarily a bias for asparagines and glutamines). Here, we examine the protein functional and interaction networks that involve prion, prionogenic and prion-like proteins. Set against a marked overall preference for N/Q-rich prion-like proteins not to interact with each other, we observe a significant tendency of prion/prionogenic proteins to interact with other, N/Q-rich prion-like proteins. This tendency is mostly due to a small number of networks involving the proteins NUP100p, LSM4p and PUB1p. In general, different data analyses of functional and interaction networks converge to indicate a strong linkage of prionogenic and prion-like proteins, to stress-granule assembly and related biological processes. These results further elucidate how prions may impact gene regulation, and reveal a broader horizon for the functional relevance of N/Q-rich prion-like domains.Djamel HarbiPaul M HarrisonPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 6, p e100615 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Djamel Harbi Paul M Harrison Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation.
description	Prions are transmissible, propagating alternative states of proteins. Prions in budding yeast propagate heritable phenotypes and can function in large-scale gene regulation, or in some cases occur as diseases of yeast. Other 'prionogenic' proteins are likely prions that have been determined experimentally to form amyloid in vivo, and to have prion-like domains that are able to propagate heritable states. Furthermore, there are over 300 additional 'prion-like' yeast proteins that have similar amino-acid composition to prions (primarily a bias for asparagines and glutamines). Here, we examine the protein functional and interaction networks that involve prion, prionogenic and prion-like proteins. Set against a marked overall preference for N/Q-rich prion-like proteins not to interact with each other, we observe a significant tendency of prion/prionogenic proteins to interact with other, N/Q-rich prion-like proteins. This tendency is mostly due to a small number of networks involving the proteins NUP100p, LSM4p and PUB1p. In general, different data analyses of functional and interaction networks converge to indicate a strong linkage of prionogenic and prion-like proteins, to stress-granule assembly and related biological processes. These results further elucidate how prions may impact gene regulation, and reveal a broader horizon for the functional relevance of N/Q-rich prion-like domains.
format	article
author	Djamel Harbi Paul M Harrison
author_facet	Djamel Harbi Paul M Harrison
author_sort	Djamel Harbi
title	Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation.
title_short	Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation.
title_full	Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation.
title_fullStr	Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation.
title_full_unstemmed	Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation.
title_sort	interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/cfab7fbcd2d64446870f7978378a3f51
work_keys_str_mv	AT djamelharbi interactionnetworksofprionprionogenicandprionlikeproteinsinbuddingyeastandtheirroleingeneregulation AT paulmharrison interactionnetworksofprionprionogenicandprionlikeproteinsinbuddingyeastandtheirroleingeneregulation
_version_	1718439352095211520

Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation.

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